Structure of PDB 4r87 Chain H

Receptor sequence
>4r87H (length=169) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
NSQLTLRALERGDLRFIHNLNNNRNIMSYWFEEPYESFDELEELYNKHIH
DNAERRFVVEDAQKNLIGLVELIEINYIHRSAEFQIIIAPEHQGKGFART
LINRALDYSFTILNLHKIYLHVAVENPKAVHLYEECGFVEEGHLVEEFFI
NGRYQDVKRMYILQSKYLN
3D structure
PDB4r87 A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.
ChainH
Resolution2.61 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.57: diamine N-acetyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 COA H Y30 I87 I88 I89 Q94 G95 G97 R100 K129 H132 Y134 Y29 I86 I87 I88 Q93 G94 G96 R99 K128 H131 Y133
BS02 SPM H N22 M28 E33 Y36 E37 E41 N21 M27 E32 Y35 E36 E40
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004145 diamine N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006598 polyamine catabolic process
GO:0046203 spermidine catabolic process
GO:0046208 spermine catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4r87, PDBe:4r87, PDBj:4r87
PDBsum4r87
PubMed25623305
UniProtQ9KL03|ATDA_VIBCH Spermidine N(1)-acetyltransferase (Gene Name=speG)

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